REGULATION OF LETHOCERUS INSECT FLIGHT MUSCLES

石斑鱼的昆虫飞行肌肉(IFM)有一块几乎是水晶的 肌节结构，并已成为许多超微结构的主题 调查。对生物化学的了解要少得多。 由此产生的单个收缩蛋白的功能和调节 肌肉。我们从石斑鱼IFM中提纯了肌球蛋白，并对其进行了研究 其在体外运动性试验中移位肌动蛋白细丝的能力。 由于一些无脊椎动物肌球蛋白受直接钙结合的调节 通过调节轻链的磷酸化而与肌球蛋白和其他物质结合 肌球蛋白的亚基，我们试图研究磷酸化在其中的作用 可以在昆虫飞行肌肉中发挥作用。不同来源的Lethocerus myosin 制剂在SDS-PAGE上显示三到四个轻链，两到三个 肌球蛋白轻链可以被肌球蛋白轻链磷酸化 或通过内源性肌球蛋白轻链激酶。的作用 目前，磷酸化仍不清楚。

The insect flight muscle (IFM) of Lethocerus has an almost crystalline sarcomere structure and has been the subject of many ultrastructural investigations. Considerably less is known about the biochemical function and regulation of the individual contractile proteins from this muscle. We have purified myosin from IFM of Lethocerus and have studied its ability to translocate actin filaments in an in vitro motility assay. Since some invertebrate myosins are regulated by direct calcium binding to the myosin and others by phosphorylation of the regulatory light chain subunit of myosin, we have tried to study what role the phosphorylation may play in insect flight muscle. Lethocerus myosin from different preparations shows three to four light chains on SDS-PAGE, two to three of which can be phosphorylated either by smooth muscle myosin light chain kinase or by an endogenous myosin light chain kinase. The role of phosphorylation is still unclear at the present time.